Abstract
α-Glucosidase from yeast is inactivated rapidly at temperatures above 42 °C. The thermal inactivation is accompanied by aggregation. The molecular chaperone GroEL suppresses the formation of aggregates by binding the thermally inactivated α-glucosidase. Spectroscopic studies suggest that GroEL binds α-glucosidase in an intermediately folded state. The complex between α-glucosidase and GroEL can be dissolved by MgATP. GroES accelerates the MgATP-dependent dissociation of the α-glucosidase-GroEL complex. At elevated temperatures this release leads to the formation of aggregates, while at lower temperatures native, enzymatically active molecules are formed.
Original language | English |
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Pages (from-to) | 11609-11614 |
Number of pages | 6 |
Journal | Biochemistry |
Volume | 30 |
Issue number | 50 |
DOIs | |
State | Published - 1 Dec 1991 |
Externally published | Yes |